We have advanced the theory that a major portion of enzymatic catalysis is achieved by activation of the substrate through binding. To support the theory, we have synthesized a large variety of test-tube models which stimulate the bound substrate by being frozen in a single, favorable conformation and by having the interacting functions brought into the closest possible juxtaposition (stereopopulation control). These compounds undergo intramolecular reactions at rates comparable to those catalyzed by enzymes, sometimes even too fast to measure. To prove that our model compounds are truly frozen in unique conformations in solution, we have initiated efforts to demonstrate that these molecules possess molecular chirality, and that the resolved enantiomers do not racemize at elevated temperatures. Furthermore, log k for enhanced cyclization is a function of the Van der Waals size of restricting groups and is independent of electronic effects.